Petite H, Rault I, Huc A, Menasche P, Herbage D
Laboratoire d'Histologie Expérimentale, U.A. CNRS 244, Université C. Bernard, Villeurbanne, France.
J Biomed Mater Res. 1990 Feb;24(2):179-87. doi: 10.1002/jbm.820240205.
Collagen biomaterials should be cross-linked in order to prevent biodegradation when they are used as implants. We have compared the cross-linking efficiencies of glutaraldehyde and acyl azide in pericardium. Glutaraldehyde is used currently, but it elicits a cytotoxic effect which reduces the biocompatibility of cross-linked tissue. We have attempted to overcome this problem by developing a cross-linking method that obviates incorporation of foreign agents. Our process involves transformation of free carboxyl groups on collagen into acyl azide groups, which react with free amino groups on adjacent side chains. We have shown that the greatest increase in the thermal stability of collagen, as measured by differential scanning calorimetry, is achieved when tissue swelling is inhibited by the addition of sodium chloride (1 M) during acyl azide formation. Under these conditions, the denaturation temperature (Td) of pericardial collagen treated with acyl azide is raised to 83.4 degrees C and that of tissue treated with glutaraldehyde to 85.1 degrees C. Moreover, acyl-azide-treated tissues have the same resistance as glutaraldehyde-treated tissues to chemical solubilization by cyanogen bromide and to enzymatic digestion by collagenase.
当胶原蛋白生物材料用作植入物时，应进行交联以防止生物降解。我们比较了戊二醛和酰基叠氮在心包中的交联效率。目前使用的是戊二醛，但它会引发细胞毒性作用，降低交联组织的生物相容性。我们试图通过开发一种避免引入外来试剂的交联方法来克服这个问题。我们的方法包括将胶原蛋白上的游离羧基转化为酰基叠氮基团，该基团与相邻侧链上的游离氨基反应。我们已经表明，通过差示扫描量热法测量，当在酰基叠氮形成过程中加入氯化钠（1M）抑制组织肿胀时，胶原蛋白的热稳定性提高最大。在这些条件下，用酰基叠氮处理的心包胶原蛋白的变性温度（Td）提高到83.4℃，用戊二醛处理的组织的变性温度提高到85.1℃。此外，酰基叠氮处理的组织与戊二醛处理的组织对溴化氰化学溶解和胶原酶酶解具有相同的抵抗力。
